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1993 | 40 | 3 |

Tytuł artykułu

Motility assay: achievements and perspectives

Warianty tytułu

Języki publikacji

EN

Abstrakty

Wydawca

-

Rocznik

Tom

40

Numer

3

Opis fizyczny

p.353-362,fig.

Twórcy

autor
  • Nencki Institute of Experimental Biology, Pasteura 3, 02-093 Warszawa, Poland

Bibliografia

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  • 2. Kron, S.J. & Spudich, J.A. (1986) Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl Acad. Sci. U.S.A. 83, 6272 - 6276.
  • 3. Sheetz, M.P. & Spudich, J.A. (1983) Movement of myosin-coated fluorescent beads on actin cables in vitro. Nature (London) 303,31 - 35.
  • 4. Sheetz, M.P., Chasan, R. & Spudich, J.A. (1984) ATP-dependent movement of myosin in vitro: Characterization of a quantitative assay. ]. Cell Biol. 99,1867-1871.
  • 5. Sellers, J.R., Spudich, J.A. & Sheetz, M.P. (1985) Light chain phosphorylation regulates the movement of smooth muscle myosin on actin filaments. J. Cell Biol. 101,1897 -1902.
  • 6. Homsher, E., Wang, F. & Sellers, J.R. (1992) Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosin. Am. J. Physiol. 262, C714 - C723.
  • 7. Sheetz, M.P., Vale, R.D., Schnapp, B.J., Schroer, T.A. & Reese, T.S. (1986) Vesicle movements and microtubule-based motors. }. Cell. Sei. (Suppl.) 5, 181 -188.
  • 8. Krön, S.J., Toyoshima, Y.Y., Uyeda, T.Q. & Spudich, J.A. (1991) Assays for actin sliding movement over myosin coated surfaces. Mäh. Enzymol. 196,399-416.
  • 9. Takiguchi, K., Hayashi, H., Kurimoto, E. & Higashi-Fujime, S. (1990) In vitro motility of skeletal muscle myosin and its proteolytic fragments. J. Biochem. (Tokyo) 107,671 - 679.
  • 10. Toyoshima, Y.Y., Krön, S.J., McNally, E.M., Niebling, K.R., Toyoshima, C. & Spudich, J.A. (1987) Myosin subfragment-1 is sufficient to move actin filaments in vitro. Nature (London) 328,536-539.
  • 11. Honda, H., Nagashima, H. & Asakura, S. (1986) Directional movement of F-actin in vitro. J. Mol. Biol. 191,131 - 133.
  • 12. Uyeda, T.Q., Kron, S.J. & Spudich, J.A. (1990) Myosin step size. Estimation from sliding movement of actin over low densities of heavy meromyosin. }. Mol. Biol. 214,699 - 710.
  • 13. Work, S.S. & Warshaw, D.M. (1992) Computer- -assisted tracking of actin filament motility. Anal. Biochem. 202,275 - 285.
  • 14. Borejdo, J. & Burlacu, S. (1992) Velocity of movement of actin filaments in vitro motility assay. Biophys. J. 61,1267- 1280.
  • 15. Hayashi, H., Takiguchi, K. & Higashi-Fujime, S. (1989) Measurement of ATPase activity of immobilized myosin heads.}. Biochem. 105,875 -877.
  • 16. Harada, Y., Noguchi, A., Kishino, A. & Yanagida, T. (1987) Sliding movement of single actin filaments on one-headed myosin filaments. Nature (London) 326,805 - 808.
  • 17. Lowey, S., Waller, G.S. & Trybus, K.M. (1993) Skeletal muscle myosin light chains are essential for movement. Biophys. J. 64,7a.
  • 18. Harrington, W.F. (1979) On the origin of the contractile force in skeletal muscle. Proc. Natl. Acad. Sci. U.S.A. 68,685 - 689.
  • 19. Sellers, J.R. & Adelstein, R.S. (1987) Regulation of contractile activity; in The Enzymes (Boyer, P.D., ed.) vol. 18, pp. 381 - 418, Academic Press, Orlando.
  • 20. Hartshorne, D.J. (1987) Biochemistry of the contractile process in smooth muscle; in Physiology of the Gastrointestinal Tract (Johnson, L.R., ed.) pp. 423 - 482, Raven Press, New York.
  • 21. Warshaw, D.M., Derosiers, J.M., Work, S.S. & Trybus, K.M. (1990) Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro. J. Cell Biol. Ill, 453 - 463.
  • 22. Okagaki, T., Higashi-Fujime, S., Ishikawa, R., Takano-Ohmuro, H. & Kohama, K. (1991) In vitro movement of actin filaments on gizzard smooth muscle myosin: Requirement of phosphorylation of myosin light chain and effects of tropomyosin and caldesmon. J. Biochem. (Tokyo) 109,858 - 866.
  • 23. Daniel, J.L., Molish, I.R. & Holmsen, H. (1981) Myosin phosphorylation in intact platelets. J. Biol. Chem. 256,7510 - 7514.
  • 24. Umemoto, S. & Sellers, J.R. (1990) Characteri­zation of in vitro motility assays using smooth muscle and cytoplasmic myosins. }. Biol. Chem. 265,14864 -14869.
  • 25. Horowitz, A. & Trybus, K.M. (1993) Inhibition of smooth muscle myosin's activity and assembly by an antirod monoclonal antilx>dy. J. Biol. Chem. 267,26091 - 26096.
  • 26. Korn, E.D. & Hammer, J.A. Ill (1990) Small myosins. Curr. Opin. Cell Biol. 2,57 - 61.
  • 27. Pollard, T.D., Doberstein, S.K. & Zot, G. (1991) Myosin-I. Annu. Rev. Physiol. 53,653 - 681.
  • 28. Zot, H.G., Doberstein, S.K. & Pollard, T.D. (1992) Myosin-I moves actin filaments on phospho­lipid surface: Implications for membrane targeting. J. Cell Biol. 116,367 - 376.
  • 29. Burton, K. (1992) Myosin step size: Estimates from motility assays and shortening muscle. J. Muscle Res. Cell Motil. 13,590 - 607.
  • 30. Yanagida, T., Arata, T. & Oosawa, F. (1985) Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle. Nature (London) 316,366 - 369.
  • 31. Harada, Y., Sakurada, K., Aoki, T., Thomas, D.D. & Yanagida, T. (1990) Mechanochemical coupling in actomyosin energy transduction studied by in vitro assay.}. Mol. Biol. 216,49 - 68.
  • 32. Uyeda, T.Q.P., Warrick, H.M., Kron, S.J. & Spudich, J.A. (1991) Quantized velocities at low myosin densities in an in vitro motility assay. Nature (London) 352,307 - 311.
  • 33. Toyoshima, Y.Y., Kron, S.J. & Spudich, J.A. (1990) The myosin step size: Measurement of the unit displacement per ATP hydrolyzed in an in vitro assay. Proc. Natl. Acad. Sei. U.S.A. 87,7130 - 7134.
  • 34. Higuchi, H. & Goldman, Y.E. (1991) Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibers. Nature (London) 352,352 - 354.
  • 35. Lombardi, V., Piazzesi, G. & Linari, M. (1992) Rapid regeneration of the actin-myosin power stroke in contracting muscle. Nature (London) 355,638 - 641.
  • 36. Kishino, A. & Yanagida, T. (1988) Force measurements by micromanipulation of a single actin filament by glass needles. Nature (London) 334,74 - 76.
  • 37. Ishijima, A., Doi, T., Sakurada, K. & Yanagida, T. (1991) Sub-piconewton force fluctuations of actomyosin in vitro. Nature (London) 352, 301 - 306.
  • 38. Toyoshima, Y.Y., Toyoshima, C. & Spudich, J.A. (1989) Bidirectional movement of actin filaments along tracks of myosin heads. Nature (London) 341,154 -156.
  • 39. Sellers, J.R. & Kachar, B. (1990) Polarity and velocity of sliding filaments: Control of dire­ction by actin and of speed by myosin. Science 249,406 - 408.
  • 40. Yamada, A. & Wakabayashi, T. (1993) Movement of actin away from the center of reconstituted rabbit myosin filament is slower than in the opposite direction: Brief commu­nication. Biophys. J. 64,565 - 569.
  • 41. Harriss, D.E. & Warshaw, D.M. (1993) Smooth and skeletal muscle actin are mechanically indistinguishable in the in vitro motility assay. Circ. Res. 72,219 - 224.
  • 42. Kron, S.J., Drubin, D.G., Botstein, D. & Spudich, J.A. (1992) Yeast actin filaments display ATP- -dependent sliding movement over surfaces coated with rabbit muscle myosin. Proc. Natl. Acad. Sä. U.S.A. 89,4466 - 4470.
  • 43. Yanagida, T. (1984) Angles of fluorescently labeled myosin heads and actin monomers in contracting and rigor stained muscle fibers; in Contractile Mechanism in Muscle (Pollack, G.H. & Sugi, H., eds.) pp. 397 - 411, Plenum Publishing Corp., New York.
  • 44. Borovikov, Yu.S. & Kąkol, I. (1991) Conforma­tional changes of contractile proteins accompanying modulation of skeletal muscle contraction. Polarized microfluorimetry investigations. Gen. Physiol. Biophys. 10, 245 - 264.
  • 45. Kąkol, I., Borovikov, Yu.S., Szczęsna, D., Kirillina, V.P. & Levitsky, D.I. (1987) Conformational changes of F-actin in myosin free ghost single fiber induced by either phosphorylated or dephosphorylated heavy meromyosin. Biochim. Biophys. Acta 913,1-9.
  • 46. Nowak, E., Borovikov, Yu.S., Khoroshev, M. & Dąbrowska, R. (1991) Troponin I and caldesmon restrict alterations in actin structure occurring on binding of myosin subfragment 1. FEBS Lett. 281,51-54.
  • 47. Oosawa, F. (1983) Macromolecular assembly of actin. Muscle Non-Muscle Motil. 1,151 - 216.
  • 48. Schutt, C.E., Lindberg, U., Myslik, J. & Strauss, N. (1989) Molecular packing in profilin:actin crystals and its implications. }. Mol. Biol. 209,735 -746.
  • 49. Schwyter, D.H., Kron, S.J., Toyoshima, Y.Y., Spudich, J.A. & Reisler, E. (1990) Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin. J. Cell. Biol. Ill, 465 - 470.
  • 50. Próchniewicz, E. & Yanagida, T. (1990) Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility. J. Mol. Biol. 216,761 - 772.
  • 51. Honda, H. & Asakura, S. (1989) Calcium- -triggered movement of regulated actin in vitro. J. Mol. Biol. 205,677 - 683.
  • 52. Williams, D.L., Greene, L.E. & Eisenberg, E. (1984) Comparison of effects of smooth and skeletal muscle tropomyosins on interaction of actin and myosin subfragment 1. Biochemistry 23,4150 - 4155.
  • 53. Walsh, M.P. (1991) Calcium-dependent mechanisms of regulation of smooth muscle contraction. Biochem. Cell Biol. 69,771 - 800.
  • 54. Shirinsky, V.P., Biryukov, K.G., Hettasch, J.M. & Sellers, J.R. (1992) Inhibition of relative movement of actin and myosin by caldesmon and calponin.}. Biol. Chem. 267,15886 - 15892.
  • 55. Ishikawa, R., Okagaki, T., Higashi-Fujime, S. & Kohama, K. (1991) Stimulation of the interaction between actin and myosin by Physarum caldesmon-like protein and smooth muscle cal­desmon. J. Biol. Chem. 266,21784 - 21790.
  • 56. Haeberle, J.R., Trybus, K.M., Hemric, M.E. & Warshaw, D.M. (1992) The effects of smoothmuscle caldesmon on actin filament motility. /. Biol. Chem. 267,23001 - 23006.
  • 57. Johara, M., Toyoshima, Y.Y., Ishijima, A., Kojima, H., Yanagida, T. & Sutoh, K. (1993) Charge-reversion mutagenesis of EHctyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion. Proc. Natl. Acad. Sci. U.S.A. 90,2127 - 2131.
  • 58. Sheperd, G.M., Corey, D.P. & Block, S.M. (1990) Actin cores of hair stereocilia support myosin motility. Proc. Natl. Acad. Sci. U.S.A. 87, 8627 - 8631.
  • 59. Nishizaka, T., Yagi, T., Tanaka, Y. & Ishiwata, S. (1993) Right-handed rotation of an actin filament in an in vitro motile system. Nature (London) 361, 269 - 271.

Typ dokumentu

Bibliografia

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Identyfikator YADDA

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